ID   LPSBP_PERAM             Reviewed;         256 AA.
AC   P26305;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Hemolymph lipopolysaccharide-binding protein;
DE            Short=LPS-BP;
DE            Short=LPS-binding protein;
DE   Flags: Precursor;
OS   Periplaneta americana (American cockroach) (Blatta americana).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Blattidae;
OC   Blattinae; Periplaneta.
OX   NCBI_TaxID=6978;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Hemolymph;
RX   PubMed=1712779; DOI=10.1016/s0021-9258(18)98841-1;
RA   Jomori T., Natori S.;
RT   "Molecular cloning of cDNA for lipopolysaccharide-binding protein from the
RT   hemolymph of the American cockroach, Periplaneta americana. Similarity of
RT   the protein with animal lectins and its acute phase expression.";
RL   J. Biol. Chem. 266:13318-13323(1991).
CC   -!- FUNCTION: Participates probably in the elimination of foreign
CC       substances invading the insect abdominal cavity, and in trapping
CC       intracellular symbionts, when they leak from the mycetomes into the
CC       hemolymph.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- INDUCTION: By introduction of foreign cells into the abdominal cavity
CC       of adult P.americana.
CC   -!- MISCELLANEOUS: Calcium is required for lipopolysaccharide binding.
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DR   EMBL; D00711; BAA00616.1; -; mRNA.
DR   PIR; A39873; JQ0708.
DR   AlphaFoldDB; P26305; -.
DR   SMR; P26305; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..33
FT                   /id="PRO_0000017542"
FT   CHAIN           34..256
FT                   /note="Hemolymph lipopolysaccharide-binding protein"
FT                   /id="PRO_0000017543"
FT   DOMAIN          146..256
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        148..252
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        230..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   256 AA;  28420 MW;  E8DF74F1AE639858 CRC64;
     MMNTRALLPL SVLLMATLCL CELPIPILQR FVRSVPEECP IADPSDFKFS ITSNRNKTGH
     WTAQVRLEHG EHEQSGSNQH NRDLWQVDLE QTTTTCAGVK SVQIITTITA PPPTAAPSIP
     PGYELSAVLG YYKFHKTPKT WDEARIICQQ EGGHLVIINS EDESKVLQNL FSKVTKTEGA
     TNNDYIFIGI HDRFVEGEFI TIFGKPLATT GFTRWVDSIQ PDNAGGNENC GSMHPNGGLN
     DIPCPWKLPF VCEVEL